123993-33-9

Upstream product

• 123993-26-0 (S)-α-<<(1,1-dimethylethoxy)carbonyl>amino>-4-(2-propenyl)benzenepropanoic acid methylester 
• 160916-46-1 N-boc-4-hydroxymethylphenylalanine 
• 216774-45-7 methyl 2-(S)-((tert-butoxycarbonyl)amino)-3-(4'-formyl-phenyl)propanoate 
• 216774-50-4 N-tert-butyloxycarbonyl-(p-hydroxymethyl)-L-phenylalanine methyl ester 
• 24424-99-5 di-tert-butyl dicarbonate 
• 1080-06-4 L-Tyr-OMe 
• 4326-36-7 (S)-N-(tert-butoxycarbonyl)tyrosine methyl ester 
• 201230-82-2 carbon monoxide 
• 112766-18-4 methyl N-(tert-butoxycarbonyl)-O-[(trifluoromethyl)sulfonyl]-L-tyrosinate 

Downstream Products

• 216774-50-4 N-tert-butyloxycarbonyl-(p-hydroxymethyl)-L-phenylalanine methyl ester 
• 160916-46-1 N-boc-4-hydroxymethylphenylalanine 

Relevant academic research and scientific papers

Agonist vs antagonist behavior of δ opioid peptides containing novel phenylalanine analogues in place of Tyr1

The novel phenylalanine analogues 4′-[N-((4′-phenyl)phenethyl) carboxamido]phenylalanine (Bcp) and 2′,6′-dimethyl-4′-[N- ((4′-phenyl)phenethyl)carboxamido]phenylalanine (Dbcp) were substituted for Tyr1 in the δ opioid antagonist TIPP (H-Tyr-Tic

Discovery of acyl guanidine tryptophan hydroxylase-1 inhibitors

An increasing number of diseases have been linked to a dysfunctional peripheral serotonin system. Given that tryptophan hydroxylase 1 (TPH1) is the rate limiting enzyme in the biosynthesis off serotonin, it represents an attractive target to regulate peripheral serotonin. Following up to our first disclosure, we report a new chemotype of TPH1 inhibitors where-by the more common central planar heterocycle has been replaced with an open-chain, acyl guanidine surrogate. Through our work, we found that compounds of this nature provide highly potent TPH1 inhibitors with favorable physicochemical properties that were effective in reducing murine intestinal 5-HT in vivo. Furthermore, we obtained a high resolution (1.90 ?) X-ray structure crystal structure of one of these inhibitors (compound 51) that elucidated the active conformation along with revealing a dimeric form of TPH1 for the first time.

COMPOSITIONS CONTAINING, METHODS INVOLVING, AND USES OF NON-NATURAL AMINO ACIDS AND POLYPEPTIDES

Disclosed herein are non-natural amino acids and polypeptides that include at least one non-natural amino acid, and methods for making such non-natural amino acids and polypeptides. The non-natural amino acids, by themselves or as a part of a polypeptide, can include a wide range of possible functionalities, but typical have at least one oxime, carbonyl, dicarbonyl, and/or hydroxylamine group. Also disclosed herein are non-natural amino acid polypeptides that are further modified post-translationally, methods for effecting such modifications, and methods for purifying such polypeptides. Typically, the modified non-natural amino acid polypeptides include at least one oximine, carbonyl, dicarbonyl, and/or hydroxylamine group. Further disclosed are methods for using such non-natural amino acid polypeptides and modified non-natural amino acid polypeptides, including therapeutic, diagnostic, and other biotechnology uses.

ACYLGUANIDINES AS TRYPTOPHAN HYDROXYLASE INHIBITORS

The present invention is directed to acylguanidines which are inhibitors of tryptophan hydroxylase (TPH), particularly isoform 1 (TPHl), that are useful in the treatment of diseases or disorders associated with peripheral serotonin including, for example, gastrointestinal, cardiovascular, pulmonary, inflammatory, metabolic, and low bone mass diseases, as well as serotonin syndrome, and cancer.

Benzoylphosphonate-based photoactive phosphopeptide mimetics for modulation of protein tyrosine phosphatases and highly specific labeling of SH2 domains

A light switch for phosphotyrosine- recognizing proteins: Irradiation of the bioisosteric benzoylphosphonate suffices to "turn off" the activity of target proteins and to label them covalently (see scheme). Photoactive bioisosters may find applications in functional cell biology, bioanalytics, and proteome research.

Total synthesis and antifungal evaluation of cyclic aminohexapeptides

The need for new therapies to treat systemic fungal infections continues to rise. Naturally occurring hexapeptide echinocandin B (1) has shown potent antifungal activity via its inhibition of the synthesis of β-1,3 glucan, a key fungal cell wall component. Although this series of agents has been limited thus far based on their physicochemical characteristics, we have found that the synthesis of analogues bearing an aminoproline residue in the 'northwest' position imparts greatly improved water solubility (>5 mg/mL). The synthesis and structure-activity relationships (SAR) based on whole cell and upon in vivo activity of the series of compounds are reported. Copyright (C) 2000 Elsevier Science Ltd.